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New protein for disease cure

Scientists have developed the first roadmap for ATP-binding cassette (ABC) transporter proteins, which are crucial components of every cell and are also involved in tumour resistance.

Scientists have struggled with understanding how ABC transporter proteins work and communicate with other proteins. Igor Stagljar, Professor in the Faculty of Medicine's Donnelly Centre for Cellular and Biomolecular Research and his team, including first author Dr. Jamie Snider, have solved the mystery by using Membrane Yeast Two-Hybrid (‘MYTH’) technology to see how these transporter proteins interact with other vital components in the cell. Stagljar, who is also cross-appointed to the Departments of Biochemistry and Molecular Genetics, said that the cell systems are complex and they need to have a solid grasp of how the individual pieces fit together in order to understand why certain diseases occur and how to best treat them.

ABC transporter proteins act as cellular gatekeepers by retaining nutrients and expelling toxins from the cell. If these proteins are not working properly, it can cause a number of diseases including: cystic fibrosis, age-related macular degeneration, Tangier disease, and Dubin-Johnson syndrome. ABC proteins can also cause cancer cells to reject chemotherapy drugs which makes treatment less effective.  Stagljar said that their discovery shows how ABC transporter proteins effect cancer and other diseases, and this knowledge can help us develop better, more targeted drugs. This is truly momentous.
Scientists chance upon

protein that can kill E. coli

Scientists at a British university have chanced up a protein that can kill the E. coli bacterium, known to cause serious food poisoning in humans. The protein Colicin N is found inside the Escherichia coli itself, and kills competing bacterium in a very efficient way. 

As part of their investigations, researchers at Newcastle University divided the protein into three parts: a receptor, which helps the protein lock-on to the bacterium; a toxic part that punches holes in the membrane of the bacterium to kill it; and a "tail-like" part.  The "tail" was thought to help the protein sneak into the cell but assumed to be harmless to the bacterium itself.

According to the researchers, they wanted to see what effect each part of the protein would have on E.coli bacteria. Amazingly when they introduced the translocation tail into the environment of the bacteria, it killed them.

Chris Johnson, a researcher who made the key discovery, said: "When I saw what had happened I didn't believe it. So we repeated it several times and the same thing happened, the bacteria died. This was certainly a result that we weren't expecting. We don't really know how this is all working so we will be looking at this in much more detail but it looks promising."

Nano-rust key to abundant production of solar hydrogen

Scientists have discovered that water and some nano-structured iron oxide is all it takes to produce bubbles of solar hydrogen.

 In the quest for the production of renewable and clean energy, photoelectrochemical cells (PECs) constitute a sort of a Holy Grail.

PECs are devices able of splitting water molecules into hydrogen and oxygen in a single operation, thanks to solar radiation.

 Michael Gratzel, Director of the Laboratory of Photonics and Interfaces (LPI) at EPFL and inventor of dye-sensitized photoelectrochemical cells, said that they have already discovered the precious chalice and have reached an important milestone on the path that will lead them forward to profitable industrial applications.

 EPFL researchers, working with Avner Rotschild from Technion (Israel), have managed to accurately characterize the iron oxide nanostructures to be used in order to produce hydrogen at the lowest possible cost.

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